Evidence map›Paper›PMID 22813742›Full record

ArticleCell reports2012

Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function.

Xiaomin Song, Bin Li, Yan Xiao, Chunxia Chen, Qiang Wang, Yujie Liu, Alan Berezov, Chen Xu, Yayi Gao, Zhiyuan Li and 8 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
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  13. Inhibition of FOXP3 by stapled alpha-helical peptides dampens regulatory T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. FOXP3 exon 2 controls TScience immunology · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors at 6 institutions in 2 countries.

Xiaomin SongState Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China 200031.
Bin Li
Yan Xiao
Chunxia Chen
Qiang Wang
Yujie Liu
Alan Berezov
Chen Xu
Yayi Gao
Zhiyuan Li
Shiaw-Lin Wu
Zheng Cai
Hongtao Zhang
Barry L Karger
Wayne W Hancock
Andrew D Wells
Zhaocai Zhou
Mark I Greene
University of Pennsylvania · USNortheastern University · USBrandeis University · USCenter for Excellence in Molecular Cell Science · CNInstitut Pasteur of Shanghai · CNShanghai Institutes for Biological Sciences · CN

Funding

Transgenic and mutant animalP01AI073489 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI KATSUMATA, MAKOTO · 2008 to 2012
$7.1M
STUDIES IN HIGH PERFORMANCE LIQUID CHROMATOGRAPHYR01GM015847 · NIGMS · NORTHEASTERN UNIVERSITY · PI KARGER, BARRY L. · 1985 to 2013
$5.7M
IMMUNOBIOLOGY OF P185 RECEPTORR01CA055306 · NCI · UNIVERSITY OF PENNSYLVANIA · PI GREENE, MARK I · 1992 to 2011
$2.6M
MECHANISTIC STUDIES OF THE HYDROLYSIS OF NUCLEOSIDESF32GM015847 · NIGMS · UNIVERSITY OF MARYLAND COLLEGE PK CAMPUS · PI MRACHKO, GREGORY T · 1993 to 1994
–
HPLC AND HPCE OF PROTEINSR37GM015847 · NIGMS · NORTHEASTERN UNIVERSITY · PI KARGER, BARRY L. · 1990 to 1999
–
NCI NIH HHS 2R01CA055306NCI NIH HHS R01 CA055306NIAID NIH HHS 5P01AI073489NIAID NIH HHS P01 AI073489NIGMS NIH HHS F32 GM015847NIGMS NIH HHS GM 15847NIGMS NIH HHS R01 GM015847NIGMS NIH HHS R37 GM015847
6 · The paper itself

Abstract

FOXP3 is a key transcription factor for regulatory T cell function. We report the crystal structure of the FOXP3 coiled-coil domain, through which a loose or transient dimeric association is formed and modulated, accounting for the activity variations introduced by disease-causing mutations or posttranslational modifications. Structure-guided mutagenesis revealed that FOXP3 coiled-coil-mediated homodimerization is essential for Treg function in vitro and in vivo. In particular, we identified human FOXP3 K250 and K252 as key residues for the conformational change and stability of the FOXP3 dimer, which can be regulated by protein posttranslational modifications such as reversible lysine acetylation. These studies provide structural and mechanistic explanations for certain disease-causing mutations in the coiled-coil domain of FOXP3 that are commonly found in IPEX syndrome. Overall, the regulatory machinery involving homooligomerization, acetylation, and heteroassociation has been dissected, defining atomic insights into the biological and pathological characteristics of the FOXP3 complex.

Indexed as

AcetylationAmino Acid SequenceAnimalsDNA Mutational AnalysisForkhead Transcription FactorsHumansJurkat CellsLeucine ZippersLysineMiceModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein Structure, SecondaryForkhead Transcription FactorsFOXP1 protein, humanFOXP3 protein, humanFoxp3 protein, mouseLysineRepressor ProteinsTransforming Growth Factor beta

Identifiers

PMID22813742
PMCPMC3401381
OpenAlexW2122434851

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.